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Histochemistry

, Volume 67, Issue 3, pp 311–319 | Cite as

Histochemical patterns in normal and splaylegged piglet muscle fibers

  • Věra Hanzlíková
Article

Summary

The histochemical pattern of muscle fiber types of the longissimus dorsi and biceps femoris muscles was investigated in normal and splaylegged piglets at birth and seven days later. Only slight differences between the muscle fibers at birth were found using histochemical reactions for alkaline adenosine triphosphatase (ATPase), succinate dehydrogenase (SDH), phosphorylase (PH) activities, and for the periodic acid-Schiff (PAS) reaction. With the method for acid-preincubated ATPase activity, high activity was observed in Type I muscle fibers and low activity in Type II muscle fibers in animals of both groups investigated. However, a higher number of Type I fibers was found in muscles of normal piglets, suggesting a faster and more advanced process of transformation of Type II into Type I muscle fibers in unaffected animals. Thus the histochemical conversion appears to be retarded in muscles of splaylegged animals, which have a histochemical pattern similar to that of normal prenatal animals. Cholinesterase activity in motor endplates was well developed; its staining revealed smaller sized and irregularly arranged endplates in muscles of affected piglets. Fiber type differentiation in muscles of animals which recovered from splayleg becomes fully developed and comparable to normal piglets seven days after birth. The number of fibers which became converted from Type II to Type I was increased; the fiber types were differentiated with regard to the PAS reaction and to their ATPase, SDH and PH activities. Morphological features of motor endplates in muscles of normal and surviving splaylegged piglets are similar.

Histochemical investigation of the fiber type differentiation thus suggests that full recovery occurs within the first week of postnatal life in muscles affected by pathological changes accompanying splayleg.

Keywords

Muscle Fiber Cholinesterase Fiber Type Phosphorylase Succinate Dehydrogenase 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag 1980

Authors and Affiliations

  • Věra Hanzlíková
    • 1
  1. 1.Institute of PhysiologyCzechoslovak Academy of SciencesPraha 4-KrčCzechoslovakia

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